Proteolytic ceramic capillary membranes for the production of peptides under flow

Antink, Marieke M. Hoog; Sewczyk, Tim; Kroll, Stephen; Árki, Pál; Beutel, Sascha; Rezwan, Kurosch; Maas, Michael

doi:10.1016/j.bej.2019.04.005

Cited by 18 publications

(17 citation statements)

References 50 publications

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“…All unwanted proteolytic side reactions of proteases and the protease hydrolysis for the acyl-enzyme during kinetic approaches are the key problems for enzymatic peptide synthesis and activity losses. The planning and optimization for enzymatic peptide synthesis always require the “S” or subsite mapping for proteases along with the knowledge of additional fundamental parameters that determined the reaction courses of proteases (Jakubke, 1994; Jäckel and Koksch, 2005; Baker and Numata, 2012; Asgher et al, 2018; Tavano et al, 2018; Antink et al, 2019; de Souza Vandenberghe et al, 2019; Mota et al, 2019; Siar et al, 2019).…”

Section: Protease Engineeringmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

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The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

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Section: Protease Engineeringmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

View full text Add to dashboard Cite

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“…Enzymatic peptide synthesis has several advantages, including enantioselectivity, free racemization, ecologically benign reaction conditions, over chemical synthesis that requires expensive defensive groups, solvents, or reagents (Agyei et al 2016 ; Antink et al 2019 ). Protease from viral, fungal, plant and animal origins has received a great deal of interest in recent years for the synthesis of many small peptides, especially dipeptides and tripeptides utilizing either a thermodynamically or a kinetically controlled bioprocess.…”

Section: Microbial Proteases and Its Industrial Applicationsmentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Putatunda²,

et al. 2021

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Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

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“…Only few studies report the use of YSZ as a support for enzyme immobilization . Often, acidic or hydrothermal hydroxylation is employed to generate more hydroxyl groups on the surface for silanization with APTES or other organosilanes . Subsequently, activation with e.g .…”

Section: Resultsmentioning

confidence: 99%

“…[36][37][38]40 Often, acidic or hydrothermal hydroxylation is employed to generate more hydroxyl groups on the surface for silanization with APTES or other organosilanes. 36,37,40 Subsequently, activation with e.g. N-hydroxysuccinimide (NHS) or 1-ethyl-3-(3-dimethylaminopropyl)carbodiimid (EDC) is followed by covalent enzyme attachment.…”

Section: Covalent Enzyme Immobilizationmentioning

confidence: 99%

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Surface treatments and functionalization of metal‐ceramic membranes for improved enzyme immobilization performance

Zeuner

Ovtar

Persson

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND Enzyme immobilization in porous membranes often improves enzyme performance. This work reports the preparation and characterization of robust and scalable asymmetric metal‐ceramic microfiltration membrane. The surface of the porous metal‐ceramic membrane was treated by impregnation with a ceramic oxide for enzyme adsorption and corrosion protection. Finally, enzyme immobilization in the support was investigated. RESULTS The bilayer membrane was successfully fabricated by combining a ceramic microfiltration layer with a metal support by tape casting, lamination and co‐sintering. A pore size in the ceramic microfiltration layer of 0.4 μm resulted in high water permeability (12 000 L/(m2 h bar)). Two different surface treatments were compared: heat treatment and yttrium(III) oxide (Y2O3) impregnation. Corrosion stability tests under enzyme‐relevant conditions gave no detectable chemical or structural changes. Alcohol dehydrogenase (EC 1.1.1.1) was immobilized in the membrane by physical adsorption and by two covalent immobilization methods. Covalent immobilization significantly improved enzyme loading, activity, and recyclability. Membrane reuse by heat treatment removed fouling, but decreased immobilization performance. CONCLUSION The improved microstructure obtained by Y2O3‐impregnation had a significant effect on enzyme loading yield and activity. This indicates the potential of this surface modification method and of these metal‐supported ceramic membranes in enzyme immobilization. Covalent immobilization was superior. © 2019 Society of Chemical Industry

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Proteolytic ceramic capillary membranes for the production of peptides under flow

Cited by 18 publications

References 50 publications

Microbial Proteases Applications

Microbial Proteases Applications

Microbial proteases: ubiquitous enzymes with innumerable uses

Surface treatments and functionalization of metal‐ceramic membranes for improved enzyme immobilization performance

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